ID   TPSDV_ABIGR             Reviewed;         868 AA.
AC   Q38710; Q94FW1;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   13-SEP-2023, entry version 116.
DE   RecName: Full=Bifunctional abietadiene synthase, chloroplastic;
DE   AltName: Full=(-)-abieta-7(8),13(14)-diene synthase;
DE   AltName: Full=Abietadiene cyclase;
DE            Short=AgAS;
DE   AltName: Full=Agggabi;
DE   Includes:
DE     RecName: Full=Abietadiene synthase;
DE              EC=4.2.3.18 {ECO:0000269|PubMed:10814381, ECO:0000269|PubMed:11112547};
DE     AltName: Full=Neoabietadiene synthase;
DE              EC=4.2.3.132 {ECO:0000269|PubMed:10814381, ECO:0000269|PubMed:11112547};
DE   Includes:
DE     RecName: Full=Copalyl diphosphate synthase;
DE              EC=5.5.1.12 {ECO:0000269|PubMed:10814381, ECO:0000269|PubMed:11112547};
DE   Flags: Precursor;
GN   Name=AS; Synonyms=ac22, ag22;
OS   Abies grandis (Grand fir) (Pinus grandis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Abies.
OX   NCBI_TaxID=46611;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 148-166; 522-530; 615-625
RP   AND 699-705, AND INDUCTION.
RC   TISSUE=Stem;
RX   PubMed=8798524; DOI=10.1074/jbc.271.38.23262;
RA   Stoffer Vogel B., Wildung M.R., Vogel G., Croteau R.B.;
RT   "Abietadiene synthase from grand fir (Abies grandis). cDNA isolation,
RT   characterization, and bacterial expression of a bifunctional diterpene
RT   cyclase involved in resin acid biosynthesis.";
RL   J. Biol. Chem. 271:23262-23268(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-868, AND NOMENCLATURE.
RX   PubMed=11404343; DOI=10.1093/genetics/158.2.811;
RA   Trapp S.C., Croteau R.B.;
RT   "Genomic organization of plant terpene synthases and molecular evolutionary
RT   implications.";
RL   Genetics 158:811-832(2001).
RN   [3]
RP   GENE FAMILY, NOMENCLATURE, AND FUNCTION.
RX   PubMed=9539701; DOI=10.1073/pnas.95.8.4126;
RA   Bohlmann J., Meyer-Gauen G., Croteau R.B.;
RT   "Plant terpenoid synthases: molecular biology and phylogenetic analysis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:4126-4133(1998).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP   REGULATION.
RX   PubMed=11112547; DOI=10.1021/bi001997l;
RA   Peters R.J., Flory J.E., Jetter R., Ravn M.M., Lee H.J., Coates R.M.,
RA   Croteau R.B.;
RT   "Abietadiene synthase from grand fir (Abies grandis): characterization and
RT   mechanism of action of the 'pseudomature' recombinant enzyme.";
RL   Biochemistry 39:15592-15602(2000).
RN   [5]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=10814381; DOI=10.1021/ol991230p;
RA   Ravn M.M., Coates R.M., Flory J.E., Peters R.J., Croteau R.;
RT   "Stereochemistry of the cyclization-rearrangement of (+)-copalyl
RT   diphosphate to (-)-abietadiene catalyzed by recombinant abietadiene
RT   synthase from Abies grandis.";
RL   Org. Lett. 2:573-576(2000).
RN   [6]
RP   MUTAGENESIS OF ASP-404 AND ASP-621, AND CHARACTERIZATION.
RX   PubMed=11552804; DOI=10.1021/ja010670k;
RA   Peters R.J., Ravn M.M., Coates R.M., Croteau R.B.;
RT   "Bifunctional abietadiene synthase: free diffusive transfer of the (+)-
RT   copalyl diphosphate intermediate between two distinct active sites.";
RL   J. Am. Chem. Soc. 123:8974-8978(2001).
RN   [7]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, 3D-STRUCTURE MODELING, AND
RP   MUTAGENESIS OF TRP-358; ASP-361; ARG-365; ASP-402; ASP-404; ASP-405;
RP   ARG-411; ARG-454; GLU-499 AND TYR-520.
RX   PubMed=11827528; DOI=10.1021/bi011879d;
RA   Peters R.J., Croteau R.B.;
RT   "Abietadiene synthase catalysis: conserved residues involved in
RT   protonation-initiated cyclization of geranylgeranyl diphosphate to (+)-
RT   copalyl diphosphate.";
RL   Biochemistry 41:1836-1842(2002).
RN   [8]
RP   MUTAGENESIS OF ARG-584; ARG-586; GLU-589; THR-617; ASP-621; ASP-625;
RP   GLU-699; SER-721; ARG-762; ASN-765; ASP-766; THR-769; GLU-773; GLU-778;
RP   TYR-841; ASP-845 AND THR-848, AND CHARACTERIZATION.
RX   PubMed=11805316; DOI=10.1073/pnas.022627099;
RA   Peters R.J., Croteau R.B.;
RT   "Abietadiene synthase catalysis: mutational analysis of a prenyl
RT   diphosphate ionization-initiated cyclization and rearrangement.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:580-584(2002).
RN   [9]
RP   FUNCTION, AND MUTAGENESIS OF LYS-86 AND ARG-87.
RX   PubMed=12614165; DOI=10.1021/bi020492n;
RA   Peters R.J., Carter O.A., Zhang Y., Matthews B.W., Croteau R.B.;
RT   "Bifunctional abietadiene synthase: mutual structural dependence of the
RT   active sites for protonation-initiated and ionization-initiated
RT   cyclizations.";
RL   Biochemistry 42:2700-2707(2003).
RN   [10]
RP   FUNCTION, AND MUTAGENESIS OF ALA-723.
RX   PubMed=18052062; DOI=10.1021/ja074977g;
RA   Wilderman P.R., Peters R.J.;
RT   "A single residue switch converts abietadiene synthase into a pimaradiene
RT   specific cyclase.";
RL   J. Am. Chem. Soc. 129:15736-15737(2007).
RN   [11]
RP   FUNCTION, AND MUTAGENESIS OF ARG-356 AND ASP-621.
RX   PubMed=20430888; DOI=10.1074/jbc.m110.123307;
RA   Mann F.M., Prisic S., Davenport E.K., Determan M.K., Coates R.M.,
RA   Peters R.J.;
RT   "A single residue switch for Mg(2+)-dependent inhibition characterizes
RT   plant class II diterpene cyclases from primary and secondary metabolism.";
RL   J. Biol. Chem. 285:20558-20563(2010).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 85-868, AND MUTAGENESIS OF
RP   ASN-451 AND VAL-727.
RX   PubMed=22219188; DOI=10.1074/jbc.m111.337592;
RA   Zhou K., Gao Y., Hoy J.A., Mann F.M., Honzatko R.B., Peters R.J.;
RT   "Insights into diterpene cyclization from structure of bifunctional
RT   abietadiene synthase from Abies grandis.";
RL   J. Biol. Chem. 287:6840-6850(2012).
CC   -!- FUNCTION: Involved in defensive oleoresin formation in conifers in
CC       response to insect attack or other injury. Involved in diterpene (C20)
CC       olefins biosynthesis. Bifunctional enzyme that catalyzes two sequential
CC       cyclizations of geranylgeranyl diphosphate (GGPP) to abietadiene. The
CC       copalyl diphosphate (CPP) intermediate diffuses freely between the 2
CC       active sites in the enzyme. Changes in reaction pH, but not salt
CC       concentration, influence the relative proportion of the major products
CC       of the enzyme, abitadiene, levopimaradiene and neoabitadiene.
CC       {ECO:0000269|PubMed:10814381, ECO:0000269|PubMed:11112547,
CC       ECO:0000269|PubMed:11827528, ECO:0000269|PubMed:12614165,
CC       ECO:0000269|PubMed:18052062, ECO:0000269|PubMed:20430888,
CC       ECO:0000269|PubMed:9539701}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = (+)-copalyl
CC         diphosphate; Xref=Rhea:RHEA:24316, ChEBI:CHEBI:58635,
CC         ChEBI:CHEBI:58756; EC=5.5.1.12;
CC         Evidence={ECO:0000269|PubMed:10814381, ECO:0000269|PubMed:11112547};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(+)-copalyl diphosphate = abieta-7,13-diene + diphosphate;
CC         Xref=Rhea:RHEA:13873, ChEBI:CHEBI:30232, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58635; EC=4.2.3.18;
CC         Evidence={ECO:0000269|PubMed:10814381, ECO:0000269|PubMed:11112547};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(+)-copalyl diphosphate = diphosphate + neoabietadiene;
CC         Xref=Rhea:RHEA:33987, ChEBI:CHEBI:29651, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58635; EC=4.2.3.132;
CC         Evidence={ECO:0000269|PubMed:10814381, ECO:0000269|PubMed:11112547};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q40577};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC   -!- ACTIVITY REGULATION: Not inhibited by 13-cyclopropylidene or 16-
CC       methylidenegeranylgeranyl diphosphate. The copalyl diphosphate synthase
CC       activity is not susceptible to magnesium-dependent inhibition.
CC       {ECO:0000269|PubMed:11112547}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3 uM for GGPP (in presence of magnesium)
CC         {ECO:0000269|PubMed:11112547, ECO:0000269|PubMed:11827528};
CC         KM=20 uM for GGPP (in absence of magnesium)
CC         {ECO:0000269|PubMed:11112547, ECO:0000269|PubMed:11827528};
CC         KM=0.4 uM for CPP (in presence of magnesium)
CC         {ECO:0000269|PubMed:11112547, ECO:0000269|PubMed:11827528};
CC         KM=10 uM for CPP (in absence of magnesium)
CC         {ECO:0000269|PubMed:11112547, ECO:0000269|PubMed:11827528};
CC       pH dependence:
CC         Optimum pH is 7.2 with GGPP as substrate and 8.7 with CPP as
CC         substrate. {ECO:0000269|PubMed:11112547,
CC         ECO:0000269|PubMed:11827528};
CC   -!- PATHWAY: Terpene metabolism; oleoresin biosynthesis.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC   -!- INDUCTION: By wounding. {ECO:0000269|PubMed:8798524}.
CC   -!- DOMAIN: The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic
CC       activity in the class II active site relevant for the cyclization of
CC       GGPP. The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the
CC       catalytic activity in the class I active site, presumably through
CC       binding to Mg(2+). {ECO:0000305}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- MISCELLANEOUS: The abietadiene synthase activity exhibits an absolute
CC       dependence on a divalent metal ion cofactor while the copalyl
CC       diphosphate synthase activity is not completely dependent.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U50768; AAB05407.1; -; mRNA.
DR   EMBL; AF326516; AAK83563.1; -; Genomic_DNA.
DR   PDB; 3S9V; X-ray; 2.30 A; A/B/C/D=85-868.
DR   PDBsum; 3S9V; -.
DR   AlphaFoldDB; Q38710; -.
DR   SMR; Q38710; -.
DR   KEGG; ag:AAB05407; -.
DR   BioCyc; MetaCyc:MONOMER-12822; -.
DR   BRENDA; 4.2.3.132; 2.
DR   BRENDA; 4.2.3.18; 2.
DR   UniPathway; UPA00924; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0050554; F:abietadiene synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050559; F:copalyl diphosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR   CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR   Gene3D; 1.50.10.160; -; 1.
DR   Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1.
DR   Gene3D; 1.50.10.130; Terpene synthase, N-terminal domain; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR044814; Terpene_cyclase_plant_C1.
DR   InterPro; IPR001906; Terpene_synth_N.
DR   InterPro; IPR036965; Terpene_synth_N_sf.
DR   InterPro; IPR005630; Terpene_synthase_metal-bd.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   PANTHER; PTHR31739; ENT-COPALYL DIPHOSPHATE SYNTHASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR31739:SF4; ENT-COPALYL DIPHOSPHATE SYNTHASE, CHLOROPLASTIC; 1.
DR   Pfam; PF01397; Terpene_synth; 1.
DR   Pfam; PF03936; Terpene_synth_C; 1.
DR   SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1.
DR   SFLD; SFLDG01604; Terpene_Cyclase_Like_1_C_Termi; 1.
DR   SFLD; SFLDG01014; Terpene_Cyclase_Like_1_N-term; 1.
DR   SFLD; SFLDG01605; Terpene_Cyclase_Like_1_N-term; 1.
DR   SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 2.
DR   SUPFAM; SSF48576; Terpenoid synthases; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chloroplast; Direct protein sequencing; Isomerase; Lyase;
KW   Magnesium; Manganese; Metal-binding; Multifunctional enzyme; Plastid;
KW   Transit peptide.
FT   TRANSIT         1..70
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           71..868
FT                   /note="Bifunctional abietadiene synthase, chloroplastic"
FT                   /id="PRO_0000033634"
FT   MOTIF           402..405
FT                   /note="DXDD motif"
FT                   /evidence="ECO:0000305"
FT   MOTIF           621..625
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000305"
FT   BINDING         269
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q38802"
FT   BINDING         402
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT   BINDING         404
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT   BINDING         489
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q38802"
FT   BINDING         621
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         621
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         625
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         625
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         765
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         769
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         773
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   MUTAGEN         86
FT                   /note="K->A: No effect on CPP binding, but decreased
FT                   abietadiene synthase activity; when associated with A-87."
FT                   /evidence="ECO:0000269|PubMed:12614165"
FT   MUTAGEN         87
FT                   /note="R->A: No effect on CPP binding, but decreased
FT                   abietadiene synthase activity; when associated with A-86."
FT                   /evidence="ECO:0000269|PubMed:12614165"
FT   MUTAGEN         356
FT                   /note="R->A: No effect on abietadiene synthase activity,
FT                   but strongly reduced copalyl diphosphate synthase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:20430888"
FT   MUTAGEN         356
FT                   /note="R->H: Increased Mg(2+) inhibition; when associated
FT                   with A-621."
FT                   /evidence="ECO:0000269|PubMed:20430888"
FT   MUTAGEN         358
FT                   /note="W->A: Decreased copalyl diphosphate synthase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:11827528"
FT   MUTAGEN         361
FT                   /note="D->A: No effect on GGPP binding, but decreased
FT                   copalyl diphosphate synthase activity."
FT                   /evidence="ECO:0000269|PubMed:11827528"
FT   MUTAGEN         365
FT                   /note="R->A: No effect on GGPP binding, but decreased
FT                   copalyl diphosphate synthase activity."
FT                   /evidence="ECO:0000269|PubMed:11827528"
FT   MUTAGEN         402
FT                   /note="D->A,E,N: No effect on GGPP binding, but decreased
FT                   copalyl diphosphate synthase activity."
FT                   /evidence="ECO:0000269|PubMed:11827528"
FT   MUTAGEN         404
FT                   /note="D->A,E,N: No effect on GGPP binding, but loss of
FT                   copalyl diphosphate synthase activity."
FT                   /evidence="ECO:0000269|PubMed:11552804,
FT                   ECO:0000269|PubMed:11827528"
FT   MUTAGEN         405
FT                   /note="D->A,E,N: No effect on GGPP binding, but decreased
FT                   copalyl diphosphate synthase activity."
FT                   /evidence="ECO:0000269|PubMed:11827528"
FT   MUTAGEN         411
FT                   /note="R->A: No effect on GGPP binding, but slightly
FT                   decreased copalyl diphosphate synthase activity."
FT                   /evidence="ECO:0000269|PubMed:11827528"
FT   MUTAGEN         451
FT                   /note="N->A: No effect on abietadiene synthase activity,
FT                   but strongly reduced copalyl diphosphate synthase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:22219188"
FT   MUTAGEN         454
FT                   /note="R->A: No effect on GGPP binding, but decreased
FT                   copalyl diphosphate synthase activity."
FT                   /evidence="ECO:0000269|PubMed:11827528"
FT   MUTAGEN         499
FT                   /note="E->A: No effect on GGPP binding, but decreased
FT                   copalyl diphosphate synthase activity."
FT                   /evidence="ECO:0000269|PubMed:11827528"
FT   MUTAGEN         520
FT                   /note="Y->A: No effect on GGPP binding, but slightly
FT                   decreased copalyl diphosphate synthase activity."
FT                   /evidence="ECO:0000269|PubMed:11827528"
FT   MUTAGEN         584
FT                   /note="R->A: No or small effect on substrate binding, but
FT                   strongly decreases abietadiene synthase activity."
FT                   /evidence="ECO:0000269|PubMed:11805316"
FT   MUTAGEN         586
FT                   /note="R->A: No or small effect on substrate binding, but
FT                   strongly decreases abietadiene synthase activity."
FT                   /evidence="ECO:0000269|PubMed:11805316"
FT   MUTAGEN         589
FT                   /note="E->A: Lower substrate binding and strong decrease of
FT                   abietadiene synthase activity."
FT                   /evidence="ECO:0000269|PubMed:11805316"
FT   MUTAGEN         617
FT                   /note="T->A: Increased production of abietadiene at the
FT                   expense of levopimaradiene."
FT                   /evidence="ECO:0000269|PubMed:11805316"
FT   MUTAGEN         621
FT                   /note="D->A: Loss of abietadiene synthase activity.
FT                   Increased Mg(2+) inhibition; when associated with H-356."
FT                   /evidence="ECO:0000269|PubMed:11552804,
FT                   ECO:0000269|PubMed:11805316, ECO:0000269|PubMed:20430888"
FT   MUTAGEN         625
FT                   /note="D->A: No or small effect on substrate binding, but
FT                   strongly decreases abietadiene synthase activity."
FT                   /evidence="ECO:0000269|PubMed:11805316"
FT   MUTAGEN         699
FT                   /note="E->A: No or small effect on substrate binding, but
FT                   strongly decreases abietadiene synthase activity."
FT                   /evidence="ECO:0000269|PubMed:11805316"
FT   MUTAGEN         721
FT                   /note="S->A: Lower substrate binding and strong decrease of
FT                   abietadiene synthase activity."
FT                   /evidence="ECO:0000269|PubMed:11805316"
FT   MUTAGEN         723
FT                   /note="A->S: Produces pimaradienes instead of
FT                   abietadienes."
FT                   /evidence="ECO:0000269|PubMed:18052062"
FT   MUTAGEN         727
FT                   /note="V->T: No effect."
FT                   /evidence="ECO:0000269|PubMed:22219188"
FT   MUTAGEN         762
FT                   /note="R->A: No or small effect on substrate binding, but
FT                   strongly decreases abietadiene synthase activity."
FT                   /evidence="ECO:0000269|PubMed:11805316"
FT   MUTAGEN         765
FT                   /note="N->A: Abolishes the conversion of CPP to
FT                   abietadiene; produces only sandaracopimaradiene."
FT                   /evidence="ECO:0000269|PubMed:11805316"
FT   MUTAGEN         766
FT                   /note="D->A: No or small effect on substrate binding, but
FT                   strongly decreases abietadiene synthase activity."
FT                   /evidence="ECO:0000269|PubMed:11805316"
FT   MUTAGEN         769
FT                   /note="T->A: Increased production of neoabietadiene at the
FT                   expense of both levopimaradiene and abietadiene."
FT                   /evidence="ECO:0000269|PubMed:11805316"
FT   MUTAGEN         773
FT                   /note="E->A: Increased production of neoabietadiene."
FT                   /evidence="ECO:0000269|PubMed:11805316"
FT   MUTAGEN         778
FT                   /note="E->A: No or small effect on substrate binding, but
FT                   strongly decreases abietadiene synthase activity."
FT                   /evidence="ECO:0000269|PubMed:11805316"
FT   MUTAGEN         841
FT                   /note="Y->F: No or small effect on substrate binding, but
FT                   strongly decreases abietadiene synthase activity."
FT                   /evidence="ECO:0000269|PubMed:11805316"
FT   MUTAGEN         845
FT                   /note="D->A: No or small effect on substrate binding, but
FT                   strongly decreases abietadiene synthase activity."
FT                   /evidence="ECO:0000269|PubMed:11805316"
FT   MUTAGEN         848
FT                   /note="T->A: No or small effect on substrate binding, but
FT                   strongly decreases abietadiene synthase activity."
FT                   /evidence="ECO:0000269|PubMed:11805316"
FT   CONFLICT        23
FT                   /note="A -> T (in Ref. 2; AAK83563)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        214
FT                   /note="F -> S (in Ref. 2; AAK83563)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        297..299
FT                   /note="DWQ -> EWE (in Ref. 2; AAK83563)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        557
FT                   /note="V -> L (in Ref. 2; AAK83563)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        579
FT                   /note="D -> E (in Ref. 2; AAK83563)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        653
FT                   /note="Q -> K (in Ref. 2; AAK83563)"
FT                   /evidence="ECO:0000305"
FT   HELIX           112..129
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           139..145
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   STRAND          155..159
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           160..168
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   STRAND          179..181
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           184..200
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           205..219
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           220..224
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           234..247
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           257..270
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           275..280
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           284..291
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   TURN            293..295
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           298..302
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           315..325
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           328..341
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           352..365
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           369..372
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           373..384
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           403..415
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           422..428
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           446..456
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           464..480
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   TURN            481..483
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   STRAND          492..494
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           496..505
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           508..510
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           513..523
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   STRAND          530..536
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   TURN            539..541
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           544..574
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   TURN            575..578
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   STRAND          581..583
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           587..597
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           601..603
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           604..624
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           630..642
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   STRAND          644..647
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           648..650
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           653..677
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           682..704
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           711..721
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           724..731
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   STRAND          735..737
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           741..744
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   TURN            745..747
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           752..776
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           782..789
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           795..819
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           824..840
FT                   /evidence="ECO:0007829|PDB:3S9V"
FT   HELIX           851..863
FT                   /evidence="ECO:0007829|PDB:3S9V"
SQ   SEQUENCE   868 AA;  99536 MW;  AD5E79F56B70D25C CRC64;
     MAMPSSSLSS QIPTAAHHLT ANAQSIPHFS TTLNAGSSAS KRRSLYLRWG KGSNKIIACV
     GEGGATSVPY QSAEKNDSLS SSTLVKREFP PGFWKDDLID SLTSSHKVAA SDEKRIETLI
     SEIKNMFRCM GYGETNPSAY DTAWVARIPA VDGSDNPHFP ETVEWILQNQ LKDGSWGEGF
     YFLAYDRILA TLACIITLTL WRTGETQVQK GIEFFRTQAG KMEDEADSHR PSGFEIVFPA
     MLKEAKILGL DLPYDLPFLK QIIEKREAKL KRIPTDVLYA LPTTLLYSLE GLQEIVDWQK
     IMKLQSKDGS FLSSPASTAA VFMRTGNKKC LDFLNFVLKK FGNHVPCHYP LDLFERLWAV
     DTVERLGIDR HFKEEIKEAL DYVYSHWDER GIGWARENPV PDIDDTAMGL RILRLHGYNV
     SSDVLKTFRD ENGEFFCFLG QTQRGVTDML NVNRCSHVSF PGETIMEEAK LCTERYLRNA
     LENVDAFDKW AFKKNIRGEV EYALKYPWHK SMPRLEARSY IENYGPDDVW LGKTVYMMPY
     ISNEKYLELA KLDFNKVQSI HQTELQDLRR WWKSSGFTDL NFTRERVTEI YFSPASFIFE
     PEFSKCREVY TKTSNFTVIL DDLYDAHGSL DDLKLFTESV KRWDLSLVDQ MPQQMKICFV
     GFYNTFNDIA KEGRERQGRD VLGYIQNVWK VQLEAYTKEA EWSEAKYVPS FNEYIENASV
     SIALGTVVLI SALFTGEVLT DEVLSKIDRE SRFLQLMGLT GRLVNDTKTY QAERGQGEVA
     SAIQCYMKDH PKISEEEALQ HVYSVMENAL EELNREFVNN KIPDIYKRLV FETARIMQLF
     YMQGDGLTLS HDMEIKEHVK NCLFQPVA
//